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Marine Lectins in Innate Immune Modulation: Mechanistic Insights, Signaling Pathways, and a Cross-Taxa Evidence Landscape. [PDF]
Mar DrugsHong CE, Lyu SY.
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Effect of Algal Lectin Siye on Proliferation and Apoptosis of Breast and Colon Cancer Cells. [PDF]
Mar DrugsZhang X +7 more
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Comparative proteomic analysis of the zebrafish (Danio rerio) perivitelline fluid; identifying putative cortical alveoli-associated proteins. [PDF]
Biol ReprodLewis BA +4 more
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Current Opinion in Structural Biology, 2020
C-type lectins are the largest and most diverse family of mammalian carbohydrate-binding proteins. They share a common protein fold, which provides the unifying basis for calcium-mediated carbohydrate recognition. Their involvement in a multitude of biological functions is remarkable.
Keller, B., Rademacher, C.
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C-type lectins are the largest and most diverse family of mammalian carbohydrate-binding proteins. They share a common protein fold, which provides the unifying basis for calcium-mediated carbohydrate recognition. Their involvement in a multitude of biological functions is remarkable.
Keller, B., Rademacher, C.
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Genomic analysis of C-type lectins
Biochemical Society Symposia, 2002Many biological effects of complex carbohydrates are mediated by lectins that contain discrete carbohydrate-recognition domains. At least seven structurally distinct families of carbohydrate-recognition domains are found in lectins that are involved in intracellular trafficking, cell adhesion, cell–cell signalling, glycoprotein turnover and innate ...
Kurt, Drickamer, Andrew J, Fadden
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C-Type Lectin Receptors in Phagocytosis
2020C-type lectin receptors (CLRs) are a family of transmembrane proteins having at least one C-type lectin-like domain (CTLD) on the cell surface and either a short intracellular signaling tail or a transmembrane domain that facilitates interaction with a second protein, often the Fc receptor common gamma chain (FcRγ), that mediates signaling.
Kai, Li, David M, Underhill
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2014
C-type lectins belong to a superfamily of receptors that share structural homology in their carbohydrate recognition domains and often bind to carbohydrates in a Ca-dependent fashion. Whereas endocytic C-type lectin receptors (CLRs) trigger the receptor-mediated endocytosis of soluble ligands, myeloid CLRs in innate immunity act as pattern recognition ...
Timo Johannssen +3 more
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C-type lectins belong to a superfamily of receptors that share structural homology in their carbohydrate recognition domains and often bind to carbohydrates in a Ca-dependent fashion. Whereas endocytic C-type lectin receptors (CLRs) trigger the receptor-mediated endocytosis of soluble ligands, myeloid CLRs in innate immunity act as pattern recognition ...
Timo Johannssen +3 more
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C-type lectin receptors in antifungal immunity
Trends in Microbiology, 2008Fungal infections represent a significant health burden, especially in immunocompromised individuals, yet many of the underlying immunological mechanisms involved in the recognition and control of these pathogens are unclear. The identification of the Toll-like receptors (TLRs) has shed new insights on innate microbial recognition and the initiation of
Janet A, Willment, Gordon D, Brown
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Current Opinion in Structural Biology, 1999
Carbohydrate-recognition domains of C-type (Ca2+-dependent) animal lectins serve as prototypes for an important family of protein modules. Only some domains in this family bind Ca2+ or sugars. A comparison of recent structures of C-type lectin-like domains reveals diversity in the modular fold, particularly in the region associated with Ca2+ and sugar ...
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Carbohydrate-recognition domains of C-type (Ca2+-dependent) animal lectins serve as prototypes for an important family of protein modules. Only some domains in this family bind Ca2+ or sugars. A comparison of recent structures of C-type lectin-like domains reveals diversity in the modular fold, particularly in the region associated with Ca2+ and sugar ...
openaire +2 more sources